S1PR2_HUMAN - dbPTM
S1PR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S1PR2_HUMAN
UniProt AC O95136
Protein Name Sphingosine 1-phosphate receptor 2
Gene Name S1PR2
Organism Homo sapiens (Human).
Sequence Length 353
Subcellular Localization Cell membrane
Multi-pass membrane protein.
Protein Description Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. When expressed in rat HTC4 hepatoma cells, is capable of mediating S1P-induced cell proliferation and suppression of apoptosis..
Protein Sequence MGSLYSEYLNPNKVQEHYNYTKETLETQETTSRQVASAFIVILCCAIVVENLLVLIAVARNSKFHSAMYLFLGNLAASDLLAGVAFVANTLLSGSVTLRLTPVQWFAREGSAFITLSASVFSLLAIAIERHVAIAKVKLYGSDKSCRMLLLIGASWLISLVLGGLPILGWNCLGHLEACSTVLPLYAKHYVLCVVTIFSIILLAIVALYVRIYCVVRSSHADMAAPQTLALLKTVTIVLGVFIVCWLPAFSILLLDYACPVHSCPILYKAHYFFAVSTLNSLLNPVIYTWRSRDLRREVLRPLQCWRPGVGVQGRRRGGTPGHHLLPLRSSSSLERGMHMPTSPTFLEGNTVV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
3Phosphorylation-----MGSLYSEYLN
-----CCCCHHHHCC		23.8827732954
5Phosphorylation---MGSLYSEYLNPN
---CCCCHHHHCCHH		10.9327732954
6Phosphorylation--MGSLYSEYLNPNK
--CCCCHHHHCCHHH		25.6727732954
8PhosphorylationMGSLYSEYLNPNKVQ
CCCCHHHHCCHHHHH		13.0727732954
19N-linked_GlycosylationNKVQEHYNYTKETLE
HHHHHHHCCCHHHHH		39.65UniProtKB CARBOHYD
24PhosphorylationHYNYTKETLETQETT
HHCCCHHHHHCCHHC		31.3029978859
27PhosphorylationYTKETLETQETTSRQ
CCHHHHHCCHHCHHH		34.5129978859
30PhosphorylationETLETQETTSRQVAS
HHHHCCHHCHHHHHH		21.9129978859
31PhosphorylationTLETQETTSRQVASA
HHHCCHHCHHHHHHH		22.5929978859
32PhosphorylationLETQETTSRQVASAF
HHCCHHCHHHHHHHH		28.3029978859
97PhosphorylationTLLSGSVTLRLTPVQ
HHHCCCEEEEEECCH		14.0924719451
142PhosphorylationAKVKLYGSDKSCRML
EEEEECCCCHHHHHH		28.4522496350
144AcetylationVKLYGSDKSCRMLLL
EEECCCCHHHHHHHH		53.837933009
305S-palmitoylationEVLRPLQCWRPGVGV
HHHHHHHCCCCCCCC		4.3629575903
320PhosphorylationQGRRRGGTPGHHLLP
CCCCCCCCCCCCCCC		28.9924702127
330PhosphorylationHHLLPLRSSSSLERG
CCCCCCCCCCCCCCC		42.1020363803
331PhosphorylationHLLPLRSSSSLERGM
CCCCCCCCCCCCCCC		19.9420363803
332PhosphorylationLLPLRSSSSLERGMH
CCCCCCCCCCCCCCC		39.9420363803
333PhosphorylationLPLRSSSSLERGMHM
CCCCCCCCCCCCCCC		35.8820363803
342PhosphorylationERGMHMPTSPTFLEG
CCCCCCCCCCCCCCC		39.5028634298
343PhosphorylationRGMHMPTSPTFLEGN
CCCCCCCCCCCCCCC		18.9728450419
345PhosphorylationMHMPTSPTFLEGNTV
CCCCCCCCCCCCCCC		40.3928450419
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of S1PR2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S1PR2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of S1PR2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CO8G_HUMANC8Gphysical
28514442
NDRG1_HUMANNDRG1physical
28514442
FKB14_HUMANFKBP14physical
28514442
PALM3_HUMANPALM3physical
28514442
SRC_HUMANSRCphysical
28514442
HPCL1_HUMANHPCAL1physical
28514442
PRAF3_HUMANARL6IP5physical
28514442
WDFY1_HUMANWDFY1physical
28514442
LEG1_HUMANLGALS1physical
28514442
KC1G3_HUMANCSNK1G3physical
28514442
PTER_HUMANPTERphysical
28514442
REEP6_HUMANREEP6physical
28514442
ATPB_HUMANATP5Bphysical
28514442
GNAQ_HUMANGNAQphysical
28514442
PPAL_HUMANACP2physical
28514442
PHAG1_HUMANPAG1physical
28514442
NEUM_HUMANGAP43physical
28514442
ARVC_HUMANARVCFphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of S1PR2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, AND MASSSPECTROMETRY.

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